Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a KrA1/4ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying protein. ZBTB44 is a 570 amino acid member of the KrA1/4ppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.
Synonyms: BTB POZ domain containing 15, BTB/POZ domain-containing protein 15, BTBD15, HSPC063, MGC26123, MGC57431, MGC60348, MGC88058, OTTHUMP00000230934, OTTHUMP00000230935, OTTHUMP00000230937, OTTHUMP00000230938, ZBT44_HUMAN, Zbtb44, Zinc finger and BTB domain containing 44, Zinc finger and BTB domain-containing protein 44, Zinc finger protein 851, ZNF851.