ALKBH1: A Protein Involved in DNA Repair and Cancer (G8846)

Target Name: ALKBH1

NCBI ID: G8846

ALKBH1: A Protein Involved in DNA Repair and Cancer

ALKBH1, also known as alkylation repair protein 1, is a protein that plays a critical role in DNA repair. It is a member of the homolog (ALK) family, which includes proteins that are involved in the repair of various types of DNA damage. One of the key functions of ALKBH1 is to repair DNA double-strand breaks, which are a common type of damage that can occur during the process of DNA replication.

ALKBH1 is a 26 kDa protein that is expressed in a variety of tissues, including muscle, heart, and brain. It is localized to the nuclei of cells and is highly conserved across different species. It has a molecular weight of 56 kDa and a calculated pI of 6.5.

The function of ALKBH1 is to repair DNA double-strand breaks. DNA double-strand breaks are caused by the formation of a physical barrier between the two complementary strands of DNA that make up a double helix. This barrier can be caused by a variety of factors, including exposure to radiation, chemical mutagenes, or errors during DNA replication. When a double-strand break occurs, the cell has several options for repairing the damage.

One of the options is to use homologs of the damaged DNA strand as a template to synthesize a new complementary strand. This process is known as homology-directed repair (HDR). In HDR, the cell uses a template that is similar to the damaged strand to synthesize a new complementary strand that can be used to replace the damaged strand.

ALKBH1 plays a key role in this process by helping the cell to locate the damaged strand on the damaged DNA molecule. It does this by using a specific domain of the protein called the N-terminus to recognize and bind to the damaged strand. Once the Damaged strand is bound, ALKBH1 helps to facilitate the formation of a new complementary strand by using its other domain, called the C-terminus, to recruit a specific enzyme called DNA polymerase.

Another way that ALKBH1 contributes to DNA repair is by helping to prevent the formation of foreign DNA sequences that can cause mutations. This is done by the protein's ability to recognize and bind to DNA sequences that are not a part of the double-strand. helps to prevent the formation of these \"mutational intermediates\" and allows the cell to maintain its genetic integrity.

In addition to its role in DNA repair, ALKBH1 is also involved in the regulation of DNA replication. It is a component of the replication complex, which is a set of proteins that work together to ensure that DNA replication is accurate and efficient. ALKBH1 helps to ensure that the replication complex is properly assembled and that the double-strand breaks are repaired before each new strand is synthesized.

The potential clinical applications of ALKBH1 as a drug target or biomarker are vast. The protein is involved in many critical processes that are necessary for human health, including DNA repair, cell growth, and reproduction. Its involvement in these processes makes it an attractive target for the development of new treatments for a variety of diseases.

One of the key potential applications of ALKBH1 is its potential as a cancer therapeutic. Double-strand breaks are a common type of cancer-causing mutation, and many treatments for cancer involve targeting these mutations. By targeting ALKBH1, researchers could potentially develop new treatments for a variety of cancers.

Another potential application of ALKBH1 is its role in the treatment of genetic disorders. ALKBH1 is involved in the regulation of DNA replication, which is a key process that is affected in many genetic disorders. For example, ALKBH1 is

Protein Name: AlkB Homolog 1, Histone H2A Dioxygenase

Functions: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:18603530, PubMed:27745969, PubMed:27497299). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:18603530, PubMed:27497299). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (PubMed:27745969, PubMed:27497299). Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (PubMed:27745969). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position (PubMed:27497299). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (PubMed:27497299). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:30392959, PubMed:30017583). N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (By similarity). Demethylates mRNAs containing N(3)-methylcytidine modification (PubMed:31188562). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (PubMed:18603530). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (PubMed:19959401). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (PubMed:19959401, PubMed:23577621). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation. May play a role in placental trophoblast lineage differentiation (By similarity)

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