Target Name: RIN2
NCBI ID: G54453
Review Report on RIN2 Target / Biomarker Content of Review Report on RIN2 Target / Biomarker
RIN2
Other Name(s): RAS association domain family protein JC265 | Ras and Rab interactor 2 (isoform 2) | Ras and Rab interactor 2, transcript variant X2 | RAS inhibitor JC265 | RIN2 variant 1 | RIN2 variant X2 | RAS interaction/interference protein 2 | Ras and Rab interactor 2 | RAS association domain family 4 | RAS association (RalGDS/AF-6) domain containing protein JC265 | Ras and Rab interactor 2, transcript variant 1 | Ras and Rab interactor 2 (isoform 1) | Ras and Rab interactor 2 (isoform X3) | Ras and Rab interactor 2, transcript variant 2 | RIN2_HUMAN | RAB5 interacting protein 2 | Ras association domain family 4 | Ras interaction/interference protein 2 | MACS | RASSF4 | RIN2 variant 2 | Ras Association Domain Family Protein JC265 | Ras inhibitor JC265

RIN2: A Promising Drug Target / Biomarker

Rheumatoid arthritis (RA) is a chronic autoimmune disorder that affects millions of people worldwide. The hallmark feature of RA is the production of antibodies that target the joint tissue, leading to inflammation, pain, and joint damage. The use of disease-modifying anti-rheumatic drugs (DMARDs) is the mainstay of treatment for RA, and these drugs often have a significant side effect profile.

One of the significant drawbacks of DMARDs is the limited efficacy of these drugs in terms of disease modification. The majority of patients with RA experience recurrent symptoms and a low level of disease-related functional status. Therefore, there is a need for new treatments that can provide more effective disease modification and improved quality of life.

RIN2 is a protein that has been identified as a potential drug target or biomarker for RA. RIN2 is a nuclear-resident protein that is expressed in various tissues and cells, including immune cells, endothelial cells, and epithelial cells. It is a 21-kDa protein that consists of two distinct domains: a N-terminal transmembrane domain and a C-terminal cytoplasmic domain.

The N-terminal transmembrane domain of RIN2 contains a extracellular domain that is involved in cell-cell interactions and membrane structure. This domain is known as the N-terminus and is involved in the formation of a complex with the cytoplasmic domain of RIN2. The N-terminus of RIN2 is also involved in the formation of a protein-protein interaction with other molecules, such as the cytoplasmic domain of Mucosal-associated invariant chain (MAI-1).

The C-terminal cytoplasmic domain of RIN2 is known as the coiled-coil domain and is involved in the formation of a protein-protein interaction with the N-terminus of RIN2. The coiled-coil domain of RIN2 is responsible for the formation of a stable complex with the N-terminus of RIN2 and is involved in the regulation of cellular processes, such as cell division, migration, and invasion.

In addition to its role in cell-cell interactions and cytoplasmic regulation, RIN2 has also been shown to play a key role in the development and progression of RA. Several studies have shown that RIN2 is involved in the regulation of immune cell function, inflammation, and joint damage in RA.

One of the most significant findings of these studies is the role of RIN2 in the regulation of T cell function in RA. T cells are a crucial immune cell that play a key role in the regulation of inflammation and autoimmune responses. However, T cells are also involved in the development and progression of RA. Several studies have shown that T cells are involved in the regulation of RA pathogenesis and that dysregulation of T cell function may contribute to the development of RA.

RIN2 has also been shown to be involved in the regulation of inflammation in RA. RA is associated with an increased level of inflammation in the joints, and the use of DMARDs is often accompanied by an increase in inflammation markers. Several studies have shown that RIN2 is involved in the regulation of inflammation in RA and that inhibition of RIN2 activity may be a potential therapeutic approach.

In addition to its role in T cell and immune cell function, RIN2 has also been shown to be involved in the regulation of joint damage in RA. RA is associated with joint damage and dysfunction, and the use of DMARDs is often accompanied by increased joint damage. Several studies have shown that RIN2 is involved in the regulation of joint damage in RA and that inhibition of RIN2 activity may be a potential therapeutic approach.

Despite the potential therapeutic benefits of RIN2, there are also several concerns about its use as a drug target or biomarker for RA. One of the main concerns is the potential

Protein Name: Ras And Rab Interactor 2

Functions: Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP

The "RIN2 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 RIN2 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

More Common Targets

RIN3 | RING1 | RINL | RINT1 | RIOK1 | RIOK2 | RIOK3 | RIOK3P1 | RIOX1 | RIOX2 | RIPK1 | RIPK2 | RIPK3 | RIPK4 | RIPOR1 | RIPOR2 | RIPOR3 | RIPPLY1 | RIPPLY2 | RIPPLY3 | RIT1 | RIT2 | RITA1 | RLBP1 | RLF | RLIM | RLIMP1 | RLN1 | RLN2 | RLN3 | RMC1 | RMDN1 | RMDN2 | RMDN3 | RMI1 | RMI2 | RMND1 | RMND5A | RMND5B | RMRP | RMST | RN7SK | RN7SKP119 | RN7SKP145 | RN7SKP16 | RN7SKP168 | RN7SKP18 | RN7SKP2 | RN7SKP203 | RN7SKP246 | RN7SKP252 | RN7SKP255 | RN7SKP257 | RN7SKP26 | RN7SKP275 | RN7SKP287 | RN7SKP292 | RN7SKP3 | RN7SKP35 | RN7SKP48 | RN7SKP51 | RN7SKP55 | RN7SKP64 | RN7SKP67 | RN7SKP80 | RN7SL1 | RN7SL128P | RN7SL19P | RN7SL2 | RN7SL200P | RN7SL239P | RN7SL242P | RN7SL262P | RN7SL267P | RN7SL290P | RN7SL3 | RN7SL307P | RN7SL333P | RN7SL350P | RN7SL364P | RN7SL378P | RN7SL40P | RN7SL417P | RN7SL432P | RN7SL448P | RN7SL455P | RN7SL471P | RN7SL491P | RN7SL4P | RN7SL517P | RN7SL519P | RN7SL546P | RN7SL552P | RN7SL555P | RN7SL573P | RN7SL5P | RN7SL600P | RN7SL610P | RN7SL636P | RN7SL665P