[6] CHID1 is expressed ubiquitously at levels nearly 6 times the average gene,[7] and is conserved very far back to organisms such as Caenorhabditis elegans and possibly some prokaryotes.

[10] Due to its large size and many exons, CHID1 has many transcript variants that have been identified through mRNA sequencing.

It has been identified in many model systems including Drosophila melanogaster, Caenorhabditis elegans, and Oryza sativa.

Another important region appears to be the last 15 amino acids, which retain a high level of conservation even through insect sequences.

The protein translation of CHID1 is typically about 400 amino acids long (though this varies within the many known forms), and has few post-translational modifications.

[16][17][18] When analyzing the promoter region of CHID1 in humans, this expression is explained by the large number of transcription factor binding sites which are active in a wide range of tissues or are even ubiquitous.

[21] The pattern of high and low expression with the brain is very similar to another widespread gene: beta actin.

[15] The function of CHID1 may also depend on its putative binding partner, STAB1, which is proposed to participate in cell signaling and defense against bacterium.

The transmembrane protein stabilin-1 has been detected as an interactant by in vitro, in vivo, and yeast two-hybrid assays.

[10] STAB1 is a large transmembrane receptor protein which may function in many aspects such as lymphocyte homing or angiogenesis.

It is expressed at over twice the average gene level and is expected to play a role in cell defense against bacterium.