Ankyrin Repeat And MYND Domain Containing 1 (ANKMY1) is a protein that in humans is encoded by the ANKMY1 gene. Known aliases of ANKMY1 include Zinc Finger

Myeloid Myeloid tissue, in the bone marrow sense of the word '' myeloid'' ('' myelo-'' + ''-oid''), is tissue of bone marrow, of bone marrow cell lineage, or resembling bone marrow, and myelogenous tissue (''myelo-'' + '' -genous'') is any tissue of, ...

, Nervy and DEAF-1 or ZMYND13.

Gene

The ANKMY1 gene is located on the minus strand of chromosome 2, at 2q37.3 . The gene begins at base position 240,479,422 and ends at position 240,577,988. The coding sequence is 3424 nucleotides long and contains 17 exons.

mRNA Expression

ANKMY1 is ubiquitously expressed in most tissue types in the body.

Protein

The ANKMY1 protein is 941 amino acids long and weighs approximately 105.5 kDa. The pI is 6.3.

Domains and motifs

ANKMY1 protein contains three MORN domains, seven ANK repeats and a single MYND zinc finger toward the end of the protein.

Structure

The ANKMY1 protein contains both beta sheets and alpha helices. The MORN domains are exclusively

beta sheet The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a g ...

s and the alpha helices appear only in the ANK domain.

Subcellular location

Subcellular location of ANKMY1 protein was found to primarily be in the cytosol. However, ANKMY1 contains nuclear export signals and evidence of nuclear transport indicating it is able to travel between both the nucleus and cytosol.

Post-translational modifications

ANKMY1 protein contains 3 sulfonated Tyrosines at positions 153, 155 and 162. There is also a N-Glycosylation sites at 163. ANKMY1 contains several (87) phosphorylation sites throughout.

Homology

Paralogs

No paralogs were found for the ANKMY1 gene.

Orthologs

ANKMY1 has numerous orthologs, strictly among vertebrates. The oldest known ortholog for ANKMY1 is the sea lamprey, an organism that diverged nearly 599 million years ago. Table 1. Orthologs of ANKMY1 in humans. Sorted first by estimated date of divergence, then by sequence identity to human protein. ANKMY1 is only found in vertebrates, not invertebrates.

Function

The specific MYND finger of ANKMY1 is specialized for protein-protein interactions. MORN repeats are also associated with linking, more specifically linking parasites and their hosts together. ANKMY1's fast evolution rate coupled with its binding capabilities make it a good candidate for cellular defense. ANKMY1 was found to interact with several proteins within the cell (Table 2).

Interacting proteins

Table 2. Potential ANKMY1 protein-protein interactions drawn from the STRING database. "N/A" indicates unknown function.

Clinical significance

Missense mutations commonly resulting in oncogenic growths were identified at various sites within the coding region. Via text-mining a link between increased expression of the ANKMY1 gene and longer time periods of metastasis-free survival in Osteosarcoma patients. ANKMY1 also shows elevated expression in the omental adipose tissue of obese children.

References

{{Reflist Zinc finger proteins