Target Name: TEX14
NCBI ID: G56155
Review Report on TEX14 Target / Biomarker Content of Review Report on TEX14 Target / Biomarker
TEX14
Other Name(s): Inactive serine/threonine-protein kinase TEX14 (isoform b) | Testis-expressed protein 14 | Inactive serine/threonine-protein kinase TEX14 | Protein kinase-like protein SgK307 | TEX14_HUMAN | Inactive serine/threonine-protein kinase TEX14 (isoform a) | protein kinase-like protein SgK307 | SGK307 | Inactive serine/threonine-protein kinase TEX14 (isoform c) | Testis expressed 14, intercellular bridge forming factor, transcript variant 1 | Testis-expressed sequence 14 | Testis-expressed sequence 14 protein | testis-expressed protein 14 | sugen kinase 307 | Testis expressed sequence 14 | testis-expressed sequence 14 protein | testis expressed 14, intercellular bridge forming factor | TEX14 variant 3 | Testis expressed 14, intercellular bridge forming factor, transcript variant 2 | SPGF23 | CT113 | Sugen kinase 307 | TEX14 variant 1 | Cancer/testis antigen 113 | TEX14 variant 2 | cancer/testis antigen 113 | Testis expressed 14, intercellular bridge forming factor, transcript variant 3

TEX14: A Potential Drug Target and Biomarker for Serine/Threonine-Protein Kinase

Abstract:

Serine/threonine-protein kinase (SPK) is a widely expressed enzyme that plays a crucial role in various cellular processes. TEX14, one of the member of the SPK family, is an inactive serine/threonine-protein kinase with unique catalytic properties. Although TEX14 has not been identified as a drug target or biomarker, its study may reveal new insights into the molecular mechanisms underlying protein kinase-mediated signaling pathways.

Introduction:

Protein kinase (PK) is a vital enzyme that catalyzes the transfer of a phosphate group from a downstream target protein to a regulatory protein. These enzymes are involved in various cellular processes, including cell growth, differentiation, and signaling pathways. The serine/threonine-protein kinase (SPK) is a subfamily of PKs that includes more than 20 different isoforms. SPKs are unique in that they not only catalyze protein-protein interactions but also regulate protein-protein interactions.

TEX14, a member of the SPK family, has unique catalytic properties that distinguish it from other SPKs. Unlike other SPKs, TEX14 is inactive, which suggests that it may not be a valid drug target or biomarker. Despite its inactive state, TEX14 is an attractive candidate for further investigation due to its unique structure and the potential it may hold for new scientific understanding.

Molecular Mechanisms:

The SPKs are a family of enzymes that share a common catalytic core, known as the catalytic domain, which consists of a catalytic center and a carboxylic acid loop. The catalytic center is the active site where the phosphate group is transferred to the regulatory protein. TEX14 is no exception to this rule.

The unique features of TEX14 lie in its catalytic properties. TEX14 has a unique N-terminus that consists of a short amino acid sequence and a hydrophobic side chain. This feature is unusual for an SPK, as it does not contain a catalytic center or any amino acids that are known to be involved in protein-protein interactions.

Furthermore, TEX14 has a unique C-terminus that is unique among SPKs. It is composed of a long amino acid sequence that includes a putative transmembrane region (TMR) and a lysine residue. This C-terminus is highly conserved among SPKs and is known to be involved in the regulation of protein-protein interactions.

Despite its unique features, TEX14 has not been identified as a drug target or biomarker. The lack of functional assays or specific inhibitors for TEX14 may be due to its limited role in cellular signaling pathways. However, its unique structure and the potential it may hold for new scientific understanding make it an attractive candidate for further investigation.

Conclusion:

In conclusion, TEX14 is a unique SPK with distinct catalytic properties. Its unusual N-terminus, C-terminus, and putative TMR suggest that it may not be a valid drug target or biomarker. However, its unique structure and the potential it may hold for new scientific understanding make it an attractive candidate for further investigation. Further studies on TEX14's role in cellular signaling pathways may reveal new insights into the molecular mechanisms underlying protein kinase-mediated signaling pathways.

Protein Name: Testis Expressed 14, Intercellular Bridge Forming Factor

Functions: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity)

The "TEX14 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 TEX14 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   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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