Target Name: SHARPIN
NCBI ID: G81858
Review Report on SHARPIN Target / Biomarker Content of Review Report on SHARPIN Target / Biomarker
SHARPIN
Other Name(s): SHANK associated RH domain interactor | shank-associated RH domain-interacting protein | SHANK associated RH domain interactor, transcript variant 1 | SHARPIN variant 1 | Shank-associated RH domain-interacting protein | SIPL1 | hSIPL1 | shank-interacting protein-like 1 | DKFZp434N1923 | SHRPN_HUMAN | Shank-interacting protein-like 1 | Sharpin

SHARPIN: A drug target and potential biomarker for SHANK associated RNA domain interactor

SHARPIN (SHank-associated RNA domain interactor) is a protein that plays a crucial role in the regulation of gene expression and has been identified as a potential drug target and biomarker. SHARPIN is a key component of the RNA polymerase II (RNA-II) complex, which is responsible for generating RNA transcripts from DNA templates in the cytoplasm of eukaryotic cells. The RNA-II complex is a complex protein-RNA binary complex that includes several subunits, including the SHARPIN protein.

The SHARPIN protein is composed of 198 amino acid residues and has a calculated molecular weight of 21 kDa. It is localized to the N-terminus of the RNA-II complex and is involved in the interactions between the RNA polymerase II subunits. SHARPIN has been shown to play a role in regulating gene expression by binding to specific DNA sequences and modulating the activity of the RNA polymerase II complex.

One of the most significant functions of SHARPIN is its ability to interact with specific DNA sequences. SHARPIN has been shown to interact with the SHC1 domain of the protein heat shock factor (HSF) and the PAS domains of the transcription factor p53. These interactions are important for the regulation of gene expression and are critical for the proper functioning of the RNA-II complex.

In addition to its role in regulating gene expression, SHARPIN has also been shown to be a potential biomarker for various diseases. For example, SHARPIN has been shown to be overexpressed in various cancer types, including breast, ovarian, and colorectal cancer. This increase in SHARPIN expression may contribute to the development and progression of these diseases.

Another potential function of SHARPIN is its role in drug discovery. SHARPIN has been shown to interact with various drugs, including small molecules, peptides, and proteins. This interaction may make SHARPIN a useful target for drug development, particularly for diseases that are currently untreated or have limited treatment options.

In conclusion, SHARPIN is a protein that has the potential to be a drug target and biomarker for various diseases. Its role in regulating gene expression and its ability to interact with specific DNA sequences make it an attractive target for drug development. Further research is needed to fully understand the functions of SHARPIN and its potential as a drug target and biomarker.

Protein Name: SHANK Associated RH Domain Interactor

Functions: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:21455173, PubMed:21455180, PubMed:21455181). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:21455173, PubMed:21455180, PubMed:21455181). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998)

The "SHARPIN 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 SHARPIN 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

SHB | SHBG | SHC1 | SHC2 | SHC3 | SHC4 | SHCBP1 | SHCBP1L | SHD | SHE | SHF | SHFL | SHH | SHISA2 | SHISA3 | SHISA4 | SHISA5 | SHISA6 | SHISA7 | SHISA8 | SHISA9 | SHISAL1 | SHISAL2A | SHISAL2B | SHKBP1 | SHLD1 | SHLD2 | SHLD2P1 | SHLD2P3 | SHLD3 | SHMT1 | SHMT2 | SHOC1 | SHOC2 | Short transient receptor potential channel (TrpC) | SHOX | SHOX2 | SHPK | SHPRH | SHQ1 | SHROOM1 | SHROOM2 | SHROOM3 | SHROOM4 | SHTN1 | SI | SIAE | SIAH1 | SIAH2 | SIAH3 | Sialidase | Sialyltransferase | SIDT1 | SIDT2 | SIGIRR | SIGLEC1 | SIGLEC10 | SIGLEC11 | SIGLEC12 | SIGLEC14 | SIGLEC15 | SIGLEC16 | SIGLEC17P | SIGLEC5 | SIGLEC6 | SIGLEC7 | SIGLEC8 | SIGLEC9 | SIGLECL1 | sigma Receptor | SIGMAR1 | Signal peptidase complex | Signal recognition particle | Signal recognition particle receptor | Signal Transducers and Activators of Transcription (STAT) | SIK1 | SIK2 | SIK3 | SIKE1 | SIL1 | SILC1 | SIM1 | SIM2 | SIMC1 | SIN3 complex | SIN3A | SIN3B | SINHCAF | SIPA1 | SIPA1L1 | SIPA1L1-AS1 | SIPA1L2 | SIPA1L3 | SIRPA | SIRPAP1 | SIRPB1 | SIRPB2 | SIRPB3P | SIRPD | SIRPG