Target Name: RBM22
NCBI ID: G55696
Review Report on RBM22 Target / Biomarker Content of Review Report on RBM22 Target / Biomarker
RBM22
Other Name(s): RNA-binding motif protein 22 | functional spliceosome-associated protein 47 | RBM22_HUMAN | Cwc2 | RNA binding motif protein 22 | zinc finger CCCH domain-containing protein 16 | fSAP47 | pre-mRNA-splicing factor RBM22 | Zinc finger CCCH domain-containing protein 16 | ZC3H16 | Pre-mRNA-splicing factor RBM22

Understanding RBM22: A RNA-Binding Motif Protein

RNA-binding motif (RBM) proteins are a family of non-protein coding RNAs that play a crucial role in various cellular processes. RBM22, also known as RNA-binding motif protein 22, is one of these RBM proteins that has gained significant interest due to its unique structure and function.

RBM22 is a 22-kDa protein that is expressed in various tissues and organs, including brain, heart, liver, and muscle. It is composed of a unique N-terminal region that contains a conserved RNA-binding motif, a central region that contains multiple functional domains, and a C-terminal region that contains a unique 3'-end structure.

The N-terminal region of RBM22 contains a conserved RNA-binding motif that is composed of the following elements: a G-Crich sequence, a D/A sequence, and a G-rich sequence that is involved in RNA-protein interactions. The D/A sequence is a crucial element for the formation of a specific RNA-protein interaction and has been implicated in the regulation of various cellular processes.

The central region of RBM22 contains multiple functional domains that are involved in the regulation of various cellular processes. The first domain is a N-terminal domain that contains a unique G/C ratio and is involved in the regulation of protein stability. The second domain is a 尾-sheet domain that is involved in the formation of beta-strands and is involved in protein stability. The third domain is a unique region that contains a G-Crich sequence and is involved in the regulation of protein stability.

The C-terminal region of RBM22 is unique and contains a 3'-end structure that is involved in the regulation of protein stability. The 3'-end region is composed of a unique G-Crich sequence that is involved in the formation of a stable RNA-protein interaction and has been implicated in the regulation of various cellular processes.

In conclusion, RBM22 is a unique and highly conserved protein that plays a crucial role in various cellular processes. The conserved RNA-binding motif and the multiple functional domains in the central region of RBM22 suggest that it may be a drug target or biomarker. Further research is needed to fully understand the unique mechanisms of RBM22 and its potential role in various cellular processes.

Protein Name: RNA Binding Motif Protein 22

Functions: Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:28502770, PubMed:28076346, PubMed:29361316, PubMed:29360106, PubMed:29301961, PubMed:30705154). Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses

The "RBM22 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 RBM22 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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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 | RDH13 | RDH14 | RDH16 | RDH5 | RDH8 | RDM1 | RDUR | RDX