KIAA1841

The molecular weight of KIAA1841 is 82 kilodaltons. The isoelectric point is 6.5. The protein sequence is not rich or low in any amino acids. There are two stretches of non-polar regions, which are capable of being transmembrane regions. There is a stretch of 21 0’s from 254-275 and a stretch of 24 0’s from 420–444.1 The DUF3342 domain stretches from 147–449.^[16]

There is an even distribution of amino acids comprising KIAA1841. The percent composition of each amino acid is fairly consistent throughout the orthologs of the protein. The most distant ortholog displays the most variance in amino acid composition. There is a higher percent composition of alanine, histidine and leucine and a lower composition of lysine.

The protein sequence of KIAA1841 is not rich or low in any amino acids. The same is true in Mus musculus, Danio rerio, Drosophila melanogaster but not true for the most distantly related. Batrachochytrium dendrobatidis is rich is histidine. Humans and closely related orthologs are composed of 2.2% to 3.8% histidine compared to 5% in Batrachochytrium dendrobatidis.

The DUF3342 domain stretches from 147-449 on KIAA1841 and has a molecular weight of 35.7 kdal. The DUF domain is low in G (2%) and rich is C (6.3%). Both of the non-polar stretches in the protein are located within the DUF domain. One at the beginning and one at the end.

The domain (DUF3342) of unknown function is a part of the pfam11822 family. This family of proteins has yet to be functionally characterized and it is found in bacteria. This domain is usually between 170 amino acids and 303 amino acids in length. The N terminal half of this protein family is a BTB-like domain. BTB domains multifunctional protein-protein interaction motif that is involved in a number of different cellular functions, including roles in regulating transcription, cytoskeleton dynamics, gating and assembly of ion channels and is involved with ubiquitination of proteins. BTB domain structures are highly conversed and are found on proteins that only have one or two other types of domains.

KIAA1841 is highly phosphorylated post modification. There are 37 predicted phosphorylated sites. There is one leucine-rich nuclear export signal toward the end of the protein. There is one sulfated tyrosine, which strengthens protein-protein interactions. Two motifs with high probability of post translational modification sumoylation sites were found. Sumoylation sites are involved in a number of cellular processes, including nuclear-cytosolic transport, transcriptional regulation and protein stability.

KIAA1841 is primarily composed of alpha helices and beta sheets. Alpha helices comprise the majority of the protein, this is true for the DUF domain and both terminuses. The DUF domain has slightly less beta sheets compared to the protein as a whole and the C terminus has an even smaller amount of beta sheets comprising its secondary structure.^[17][18]

Protein KIAA1841 is targeted to the nucleus.^[19]

KIAA1841 was found to interact with SRPK1 (Serine/arginine- rich protein-specific kinase 1)^[20] The interaction was detected via a protein kinase assay. SRPK1 localizes to the nucleus and the cytoplasm. By regulating intracellular localization of splicing factors it is thought to play a role in regulating both constitutive and alternative splicing. KIAA1841 is also found in the nucleus and is thought to play a role in regulating transcription.

Diseases associated with this gene are Crohn’s disease, celiac disease and inflammatory bowel disease.^[21][22]