Target Name: RBM15
NCBI ID: G64783
Review Report on RBM15 Target / Biomarker Content of Review Report on RBM15 Target / Biomarker
RBM15
Other Name(s): putative RNA-binding protein 15 | FLJ12479 | RBM15_HUMAN | One twenty-two | one twenty-two | RBM15 variant 1 | One twenty two protein | RNA binding motif protein 15, transcript variant 2 | SPEN | MGC119584 | one twenty two protein | RNA-binding motif protein 15 | OTTHUMP00000013007 | RNA-binding protein 15 (isoform 1) | OTT | FLJ21943 | RNA-binding protein 15 (isoform 2) | One-twenty two protein 1 | RNA binding motif protein 15 | RNA-binding protein 15 | RBM15 variant 2 | RNA binding motif protein 15, transcript variant 1 | OTT1 | one-twenty two protein 1

RBM15: A Potential Drug Target and Biomarker for Positive Impact on RNA-Binding Proteins

Abstract:

RBM15, a putative RNA-binding protein, has been identified as a potential drug target and biomarker for various diseases. Its unique structure and function make it an attractive target for the development of new therapeutics. This article will discuss the characterization of RBM15, its potential drug targets, and its potential as a biomarker for disease diagnosis and progression.

Introduction:

RBM15, also known as P150, is a protein that contains a unique N-terminal domain with high homophilic interaction potential. This domain is known as the N-terminal alpha-helicase domain (NAD) and is responsible for the protein's N-terminal localization to the endoplasmic reticulum (ER) and its subsequent stability in the ER. Additionally, RBM15 has a unique C-terminal region that contains a conserved G-rich sequence, which is known as the N-terminal G-rich region (NGRR).

RBM15 has been shown to play a crucial role in various cellular processes, including cell adhesion, migration, and the regulation of gene expression. Its unique structure and function make it an attractive target for the development of new therapeutics.

Characterization of RBM15:

The N-terminal domain of RBM15 is characterized by a unique alpha-helicase domain (NAD) that contains a variable number of conserved amino acids with a conserved Asp209 and Asn210. The NAD is responsible for the protein's N-terminal localization to the ER and its subsequent stability in the ER.

The C-terminal region of RBM15 is characterized by a conserved G-rich sequence (NGRR), which is known to play a crucial role in the protein's stability and localization to the ER. Additionally, the C-terminal region contains a conserved Glu221 and a conserved Asp222, which are involved in the N-terminal localization of RBM15 to the ER.

Potential Drug Targets:

RBM15 has been shown to play a crucial role in various cellular processes, including cell adhesion, migration, and the regulation of gene expression. Its unique structure and function make it an attractive target for the development of new therapeutics.

One of the potential drug targets for RBM15 is the inhibition of its N-terminal domain, which has been shown to play a role in the stability and localization of RBM15 to the ER. This can be achieved by inhibiting the activity of the NAD, which is responsible for the stability of RBM15 in the ER.

Another potential drug target for RBM15 is the inhibition of its C-terminal domain, which has been shown to play a role in the stability and localization of RBM15 to the ER. This can be achieved by inhibiting the activity of the NGRR, which is responsible for the localization of RBM15 to the ER.

Potential Biomarker:

RBM15 has the potential to serve as a biomarker for various diseases, including cancer, neurodegenerative diseases, and respiratory diseases. Its unique structure and function make it an attractive target for the development of new diagnostic tools and therapeutic agents.

One of the potential biomarkers for RBM15 is its expression level in various tissues and fluids, such as urine, plasma, and tissue samples. This can be used as a

Protein Name: RNA Binding Motif Protein 15

Functions: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311)

The "RBM15 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about RBM15 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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RBM15-AS1 | RBM15B | RBM17 | RBM17P1 | RBM18 | RBM19 | RBM20 | RBM22 | RBM22P1 | RBM23 | RBM24 | RBM25 | RBM26 | RBM26-AS1 | RBM27 | RBM28 | RBM3 | RBM33 | RBM34 | RBM38 | RBM39 | RBM4 | RBM41 | RBM42 | RBM43 | RBM43P1 | RBM44 | RBM45 | RBM46 | RBM47 | RBM48 | RBM48P1 | RBM4B | RBM5 | RBM5-AS1 | RBM6 | RBM7 | RBM8A | RBMS1 | RBMS1P1 | RBMS2 | RBMS2P1 | RBMS3 | RBMS3-AS3 | RBMX | RBMX2 | RBMX2P1 | RBMXL1 | RBMXL2 | RBMXL3 | RBMY1A1 | RBMY1B | RBMY1D | RBMY1F | RBMY1J | RBMY2EP | RBMY2FP | RBP1 | RBP2 | RBP3 | RBP4 | RBP5 | RBP7 | RBPJ | RBPJL | RBPJP2 | RBPMS | RBPMS-AS1 | RBPMS2 | RBSN | RBX1 | RC3H1 | RC3H2 | RCAN1 | RCAN2 | RCAN3 | RCAN3AS | RCBTB1 | RCBTB2 | RCC1 | RCC1L | RCC2 | RCCD1 | RCE1 | RCHY1 | RCL1 | RCN1 | RCN1P2 | RCN2 | RCN3 | RCOR1 | RCOR2 | RCOR3 | RCSD1 | RCVRN | RD3 | RD3L | RDH10 | RDH11 | RDH12