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KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

PNPLA2 is an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Mutations in the PNPLA2 gene are linked to neutral lipid storage disease with myopathy.

KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.

Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.