EBNA1BP2: A Potential Drug Target and Biomarker for rRNA Processing in Cancer

Target Name: EBNA1BP2

NCBI ID: G10969

EBNA1BP2: A Potential Drug Target and Biomarker for rRNA Processing in Cancer

Abstract:

EBNA1BP2, a member of the heat shock protein (HSP) family, is a protein that plays a critical role in the regulation of rRNA processing in the nucleus. Its function in rRNA processing has been studied extensively, and its potential as a drug target or biomarker in cancer is highly evaluated. This article aims to provide a comprehensive overview of EBNA1BP2, including its structure, function, and potential as a drug target or biomarker in cancer.

Introduction:

RNA is the most abundant protein in the cell, and it plays a critical role in gene expression and cellular signaling. The regulation of RNA processing is a critical aspect of gene expression, and the protein EBNA1BP2 plays a crucial role in this process in the nucleus . EBP2 is a heat shock protein (HSP) that is expressed in a variety of tissues and cells, including the brain, heart, liver, and cancer cells. It has a critical role in the regulation of rRNA processing in the nucleus, and its function in this process has been extensively studied.

Structure and Function:

EBP2 is a 23.8 kDa protein that contains 115 amino acid residues. It has a molecular weight of 21.1 kDa and a calculated pI of 6.3. EBP2 is a monomeric protein that consists of a unique N-terminal region, a catalytic domain, and a C -terminal region that contains a putative N-end domain (NED) and a C-end domain (CED).

The N-terminal region of EBP2 contains a 25 amino acid residue protein domain that includes a nucleotide-binding oligomerization (NBO) domain and a leucine-rich repeat (LRR) domain. The NBO domain is a common protein domain that is involved in various cellular processes, including DNA replication, transcription, and RNA processing. The LRR domain is a unique protein domain that is involved in protein-protein interactions and is characterized by a specificity for alpha-helices.

The catalytic domain of EBP2 contains a single alpha-helical domain that is responsible for its catalytic activity. The alpha-helical structure of the catalytic domain is stable and allows EBP2 to interact with other proteins and RNA molecules in a specific way.

The C-terminal region of EBP2 contains a 13 amino acid residue protein domain that includes a putative N-end domain (NED) and a C-end domain (CED). The NED is a unique protein domain that is involved in various cellular processes , including protein-protein interactions and cell signaling. The CED is a common protein domain that is involved in protein-protein interactions and is characterized by a specificity for beta-helices.

EBP2's Putative N-End Domain:

The N-end domain of EBP2 is a unique protein domain that is involved in various cellular processes, including protein-protein interactions and cell signaling. The N-end domain is a critical region of EBP2 that is involved in the regulation of rRNA processing in the nucleus.

The N-end domain of EBP2 is characterized by a specificity for alpha-helices. Alpha-helices are short, linear protein regions that are characterized by a specific sequence of amino acids. The N-end domain of EBP2 is involved in the regulation of alpha-helices, which are important for protein-protein interactions and

Protein Name: EBNA1 Binding Protein 2

Functions: Required for the processing of the 27S pre-rRNA

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