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BZIP domain

Protein domain From Wikipedia, the free encyclopedia

BZIP domain
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The Basic Leucine Zipper Domain (bZIP domain) is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors.[1][2]

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bZIP transcription factors

bZIP transcription factors are found in all eukaryotes and form one of the largest families of dimerizing TFs.[3] An evolutionary study from 2008 revealed that 4 bZIP genes were encoded by the genome of the most recent common ancestor of all plants.[4] Interactions between bZIP transcription factors are numerous and complex [5][6][3] and play important roles in cancer development[7] in epithelial tissues, steroid hormone synthesis by cells of endocrine tissues,[8] factors affecting reproductive functions,[9] and several other phenomena that affect human health.

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bZIP domain containing proteins

Human proteins containing this domain

ATF1; ATF2; ATF4; ATF5; ATF6; ATF7; BACH1; BACH2; BATF; BATF2; CEBPA; CEBPB; CEBPD; CEBPE; CEBPG; CEBPZ; CREB1; CREB3; CREB3L1; CREB3L2; CREB3L3; CREB3L4; CREB5; CREBL1; CREM; E4BP4; FOSL1; FOSL2; JUN; JUNB; JUND; MAFA; MAFB; MAFF; MAFG; NRL; C-MAF; MAFK; NFE2; NFE2L2; NFE2L3; SNFT; XBP1

References

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