Target Name: BOD1L2
NCBI ID: G284257
Other Name(s): putative biorientation of chromosomes in cell division protein 1 pseudogene | Putative protein FAM44C | Biorientation of chromosomes in cell division protein 1-like 2 | family with sequence similarity 44, member C | Protein FAM44C | biorientation of chromosomes in cell division 1 pseudogene | Biorientation of chromosomes in cell division protein 1 pseudogene | biorientation of chromosomes in cell division protein 1 pseudogene | Biorientation of chromosomes in cell division 1 like 2 | putative protein FAM44C | BD1L2_HUMAN | Putative biorientation of chromosomes in cell division protein 1 pseudogene | Family with sequence similarity 44, member C | Biorientation of chromosomes in cell division 1 pseudogene | FAM44C | BOD1P | Putative biorientation of chromosomes in cell division protein 1-like 2 | biorientation of chromosomes in cell division 1 like 2 | putative biorientation of chromosomes in cell division protein 1-like 2

BOD1L2: A Potential Drug Target and Biomarker for Cell Division Protein 1 Pseudogene

Chromosomal instability (CIN) is a hallmark of cancer, and it is a crucial factor in the development of most diseases. Chromosomal instability is caused by various mechanisms, including DNA damage, errors in DNA replication, and changes in gene expression. One of the key proteins involved in the regulation of chromosomal stability is Cell Division Protein 1 (CDP1). CDP1 is a transmembrane protein that plays a crucial role in the maintenance of chromosomal stability during cell division. CDP1 functions by interacting with the sister chromatids and preventing their separation during mitosis and meiosis.

Putative pseudogene

The putative pseudogene of CDP1, BOD1L2, is a gene that encodes a protein with similar sequences to CDP1. The BOD1L2 gene was identified in various organisms, including humans, using DNA sequencing technology. The BOD1L2 protein has a predicted localization to the endoplasmic reticulum (ER) and is expressed in various tissues, including brain, heart, and muscle.

CDP1 and BOD1L2

CDP1 is a 21-kDa protein that is expressed in various tissues and is involved in the regulation of chromosomal stability. BOD1L2 is a pseudogene that encodes a protein with similar sequences to CDP1. The primary structure of BOD1L2 is similar to CDP1, but the BOD1L2 protein has a different reading frame and a different protein length.

BOD1L2 function

BOD1L2 functions as a negative regulator of CDP1. It prevents CDP1 from interacting with the sister chromatids and thereby prevents the separation of the sister chromatids during cell division. BOD1L2 functions by binding to a specific region of CDP1 and preventing it from interacting with the sister chromatids.

Drug targeting

BOD1L2 is a potential drug target for the treatment of various diseases. One of the reasons for its potential as a drug target is its involvement in the regulation of chromosomal stability. By targeting BOD1L2, researchers can disrupt the function of CDP1 and prevent the regulation of chromosomal stability, leading to the development of various diseases.

BOD1L2 as a biomarker

BOD1L2 can also be used as a biomarker for the diagnosis and monitoring of various diseases. For example, BOD1L2 can be used as a biomarker for the treatment of leukemia, a type of cancer that affects the bone marrow. In leukemia, the expression of CDP1 is often increased, and BOD1L2 can be used as a tool to identify patients who are responsive to a particular treatment.

Conclusion

In conclusion, BOD1L2 is a putative drug target and biomarker for the regulation of chromosomal stability. Its functions as a negative regulator of CDP1 and its potential as a drug target make it an attractive target for the development of new therapies for various diseases. Further research is needed to fully understand the role of BOD1L2 in the regulation of chromosomal stability and its potential as a drug target and biomarker.

Protein Name: Biorientation Of Chromosomes In Cell Division 1 Like 2

Functions: May play a role in proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles

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