# FAM193A

## Overview
FAM193A, or Family with Sequence Similarity 193 Member A, is a gene located on human chromosome 8 that encodes a protein of the same name. While the specific functions of the FAM193A protein are not fully characterized, it is known to be involved in various cellular processes, potentially including development, bone health, and cancer progression. The protein is implicated in protein-protein interactions, which are crucial for cellular regulation and response mechanisms. Despite its unclear role in normal physiology, mutations and alterations in FAM193A have been associated with several medical conditions, such as mild Wolf-Hirschhorn Syndrome, thymoma, and medication-induced osteonecrosis of the jaw, highlighting its potential importance in disease mechanisms and therapeutic responses (Hannes2012A; Lee2019Identifying; Belani2014ASXL1).

## Function
The specific molecular functions and roles of the FAM193A protein in healthy human cells are not well-characterized in the available scientific literature. However, studies have implicated the gene in various health conditions, suggesting its potential involvement in broader cellular processes. For instance, a microdeletion including FAM193A has been associated with mild Wolf-Hirschhorn Syndrome, indicating that the gene might contribute to the phenotype either through regulatory sequences affecting gene expression in critical regions or by adding to the phenotypic expression when combined with deletions of critical regions (Hannes2012A). Additionally, a frameshift mutation in FAM193A described as 'damaging' was identified in a patient with a B3 thymoma, suggesting a possible role in tumorigenesis or progression of the thymoma (Belani2014ASXL1). Furthermore, FAM193A was found to be significantly enriched in a group of patients with medication-induced osteonecrosis of the jaw, hinting at its involvement in disease mechanisms specific to bone pathology (Lee2019Identifying). These associations suggest that FAM193A may play a role in cellular processes relevant to development, bone health, and possibly cancer, although direct functions in normal cellular physiology remain to be fully elucidated.

## Clinical Significance
FAM193A has been implicated in various medical conditions through mutations, altered expression levels, or disruptions in its normal interactions. Notably, a study identified a significant association between FAM193A and bisphosphonate-induced osteonecrosis of the jaw (BRONJ) in patients treated for osteoporosis, suggesting a genetic predisposition that affects the response to bisphosphonate therapy (Lee2019Identifying). Additionally, FAM193A mutations have been utilized as markers in the analysis of minimal residual disease (MRD) in acute myeloid leukemia (AML). Variants in FAM193A were tracked to monitor mutation loads during treatment, correlating with patient MRD levels, which indicates its potential role in the progression and treatment response of AML (Malmberg2016Patient‐tailored).

Furthermore, FAM193A is part of a microdeletion proximal to the Wolf-Hirschhorn Syndrome Critical Region, associated with a mild Wolf-Hirschhorn Syndrome (WHS) facial phenotype. This suggests that deletions affecting FAM193A may contribute to the phenotypic expression of WHS, particularly in combination with deletions in critical regions (Hannes2012A). These findings underscore the clinical significance of FAM193A in contributing to the pathology of diverse conditions, ranging from genetic syndromes like WHS to treatment-related adverse effects such as BRONJ.

## Interactions
FAM193A, or Family with Sequence Similarity 193 Member A, encodes a protein that is implicated in various cellular processes through its involvement in protein-protein interactions. These interactions are essential for numerous biological functions, including signal transduction, cellular regulation, and immune responses. The protein encoded by FAM193A can participate in both stable and transient interactions, which are critical for forming protein complexes and regulatory mechanisms, respectively.

Although specific interaction partners and the exact nature of these interactions (whether activating or inhibitory) for FAM193A are not detailed in the available literature, the general role of such proteins suggests that FAM193A could interact with other proteins or nucleic acids to influence cellular functions. These interactions typically involve molecular docking, where physical contacts are established between the FAM193A protein and other molecular entities, facilitating the regulation of cellular pathways and processes.

Understanding the interactions of FAM193A is crucial for elucidating its function in cellular biology, particularly how it contributes to the regulation of cellular mechanisms and responses to environmental signals.


## References


[1. (Hannes2012A) Femke Hannes, Peter Hammond, Oliver Quarrell, Jean‐Pierre Fryns, Koenraad Devriendt, and Joris R. Vermeesch. A microdeletion proximal of the critical deletion region is associated with mild wolf–hirschhorn syndrome. American Journal of Medical Genetics Part A, 158A(5):996–1004, March 2012. URL: http://dx.doi.org/10.1002/ajmg.a.35299, doi:10.1002/ajmg.a.35299. (23 citations) 10.1002/ajmg.a.35299](https://doi.org/10.1002/ajmg.a.35299)

[2. (Lee2019Identifying) Kye Hwa Lee, Su-Hwan Kim, Chang Hyen Kim, Byung Joo Min, Grace Juyun Kim, Younggyun Lim, Hun-Sung Kim, Kang-Min Ahn, and Ju Han Kim. Identifying genetic variants underlying medication-induced osteonecrosis of the jaw in cancer and osteoporosis: a case control study. Journal of Translational Medicine, November 2019. URL: http://dx.doi.org/10.1186/s12967-019-2129-3, doi:10.1186/s12967-019-2129-3. (25 citations) 10.1186/s12967-019-2129-3](https://doi.org/10.1186/s12967-019-2129-3)

[3. (Belani2014ASXL1) R Belani, G Oliveira, G A Erikson, S Ra, M S Schechter, J K Lee, W J Shipman, S M Haaser, and A Torkamani. Asxl1 and dnmt3a mutation in a cytogenetically normal b3 thymoma. Oncogenesis, 3(7):e111–e111, July 2014. URL: http://dx.doi.org/10.1038/oncsis.2014.25, doi:10.1038/oncsis.2014.25. (20 citations) 10.1038/oncsis.2014.25](https://doi.org/10.1038/oncsis.2014.25)

[4. (Malmberg2016Patient‐tailored) Erik B.R. Malmberg, Sara Ståhlman, Anna Rehammar, Tore Samuelsson, Sofie J. Alm, Erik Kristiansson, Jonas Abrahamsson, Hege Garelius, Louise Pettersson, Mats Ehinger, Lars Palmqvist, and Linda Fogelstrand. Patient‐tailored analysis of minimal residual disease in acute myeloid leukemia using next‐generation sequencing. European Journal of Haematology, 98(1):26–37, June 2016. URL: http://dx.doi.org/10.1111/ejh.12780, doi:10.1111/ejh.12780. (35 citations) 10.1111/ejh.12780](https://doi.org/10.1111/ejh.12780)