Zinc finger SWIM-type containing protein 4 (ZSWIM4)

Zinc finger SWIM-type containing protein 4 (ZSWIM4) is a member of the ZSWIM family of proteins, characterized by the presence of a SWIM-type zinc finger domain, which confers DNA- and protein-binding capabilities[1][3]. ZSWIM4 is localized to the nucleus and predicted to function as a substrate adaptor in E3 ubiquitin ligase complexes, specifically Cul2-RING ligase assemblies, by forming complexes with Elongin B, Elongin C, and CUL2[2][3][4]. Functionally, ZSWIM4 attenuates BMP (bone morphogenic protein) signaling during embryonic patterning by promoting nuclear ubiquitination and degradation of SMAD1[2]. It is expressed across multiple tissues, with elevated levels reported in the brain and kidney[1]. While ZSWIM4 has been implicated as required for JAK2 inhibition resistance in breast cancer, there is no current evidence of direct drug targeting or biomarker usage in a clinical context[5]. Its main identified biological roles are in protein ubiquitination, negative regulation of BMP signaling, and embryonic developmental patterning[1][2].

Other names

FLJ12221ZSWIM4