TRIM7 Regulates SPS Pathway By Ensuring Proper SMAS Levels (G81786)

Target Name: TRIM7

NCBI ID: G81786

TRIM7

TRIM7 Regulates SPS Pathway By Ensuring Proper SMAS Levels

TRIM7 (TRIM7_HUMAN), a protein that belongs to the TRIM7 family, is a key regulator of the terminal sphingomyelin sulfate (SMAS) synthetase, a critical step in the intracellular signaling pathway known as the Sphingolipid Signaling (SPS) pathway. The SPS pathway is involved in the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of SPS pathway by ensuring the proper levels of SMAS, which is a major signaling molecule in the SPS pathway.

TRIM7 is a 7-kDa protein that consists of an N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop region. The N-terminal transmembrane domain is responsible for the protein's ability to interact with various membrane receptors, including the SMAS receptor, while the catalytic domain is responsible for the protein's catalytic activity. The C-terminal T-loop region is involved in the regulation of the SPS pathway by interacting with the protein p150, which is a component of the SMAS complex.

The SPS pathway is a critical pathway involved in the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of this pathway by ensuring the proper levels of SMAS. SMAS is a major signaling molecule in the SPS pathway that is involved in the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of the SPS pathway by ensuring the proper levels of SMAS.

TRIM7 is involved in the regulation of the SPS pathway by interacting with the protein p150. The p150 protein is a component of the SMAS complex, which is responsible for the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of the SPS pathway by interacting with the protein p150, which is a component of the SMAS complex.

The TRIM7 protein is also involved in the regulation of cellular signaling pathways. The SPS pathway is involved in the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of these pathways by ensuring the proper levels of SMAS, which is a major signaling molecule in the SPS pathway.

In conclusion, TRIM7 (TRIM7_HUMAN) is a protein that is involved in the regulation of various cellular processes, including cell signaling, cell survival, and cell inflammation. The TRIM7 protein plays a crucial role in the regulation of the SPS pathway by ensuring the proper levels of SMAS, which is a major signaling molecule in the pathway. Further research is needed to fully understand the role of TRIM7 in the regulation of cellular processes.

Protein Name: Tripartite Motif Containing 7

Functions: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration (PubMed:25851810, PubMed:32853985, PubMed:34062120). Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and NSP8 proteins (PubMed:34062120, PubMed:35982226). Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation (PubMed:35982226, PubMed:35867826, PubMed:35893676). Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (PubMed:25851810). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (By similarity). Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation (PubMed:32126128). Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1 (PubMed:32853985). Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation (PubMed:36067704)

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