Category: Database: Gene/Protein

The Chromosomal Passenger Complex (CPC) is a dynamic mitotic regulator composed of Aurora B, INCENP, Borealin and Survivin. It ensures accurate chromosome segregation, corrects spindle attachment errors and coordinates cytokinesis, making it essential for genomic stability and highly relevant in cancer biology.

Survivin (BIRC5) is a tumour‑specific IAP that integrates apoptosis suppression with essential mitotic functions. As part of the chromosomal passenger complex, Survivin ensures proper chromosome segregation while stabilising anti‑apoptotic pathways, making it a central driver of tumour progression and therapy resistance.

NAIP is a pattern‑recognition receptor that detects bacterial ligands such as flagellin and type III secretion system proteins. By recruiting NLRC4 to form the NAIP–NLRC4 inflammasome, NAIP activates caspase‑1, triggers pyroptosis and drives early innate immune defence against intracellular pathogens.

Livin (ML‑IAP) is a tumour‑specific inhibitor of apoptosis that blocks caspase activity and ubiquitinates pro‑apoptotic proteins. Its splice variants, Livin‑α and Livin‑β, differ in potency, and its unique ability to switch from anti‑apoptotic to pro‑apoptotic after cleavage makes Livin a key regulator of tumour survival and therapy resistance.

cIAP2 is a ubiquitin ligase that regulates TNF receptor signalling, non‑canonical NF‑κB activation and NOD2‑mediated immune responses. By controlling RIPK1, RIPK2 and NIK stability, cIAP2 determines whether cells activate survival pathways or transition into apoptosis, making it essential in inflammation and cancer biology.

cIAP1 is a ubiquitin ligase that regulates TNF receptor signalling and determines whether cells activate NF‑κB survival pathways or switch into apoptosis or necroptosis. By controlling RIPK1 ubiquitination and cooperating with TRAF2, cIAP1 plays essential roles in inflammation, immunity and cancer biology.

TRIM21 is a unique intracellular antibody receptor and RING finger ubiquitin ligase that neutralises antibody‑coated viruses inside the cytosol. Through its PRY/SPRY domain and tripartite motif, TRIM21 triggers rapid ubiquitin‑mediated degradation and activates antiviral signalling pathways. Its roles in immunity, autoimmunity and biotechnology make TRIM21 a key regulator of intracellular defence.

TRIM25 is a RING finger ubiquitin ligase that activates the antiviral sensor RIG‑I through K63‑linked ubiquitination. Its tripartite motif and PRY/SPRY domain enable precise regulation of innate immune signalling, interferon production and viral restriction. TRIM25 is targeted by multiple viruses, highlighting its importance as a frontline antiviral factor.

The TRIM family is a large group of single‑chain RING finger ubiquitin ligases that regulate innate immunity, antiviral defence, autophagy, transcription and protein quality control. Defined by their tripartite motif—RING, B‑box and coiled‑coil domains—TRIM proteins use diverse C‑terminal regions to achieve precise substrate specificity. Their roles in immunity, development and cancer make them key regulators of cellular homeostasis.

Cbl‑c is an epithelial‑specific RING finger ubiquitin ligase that regulates EGFR and other receptor tyrosine kinases through targeted ubiquitination. With a streamlined domain architecture and restricted expression pattern, Cbl‑c maintains epithelial homeostasis and prevents excessive RTK signalling. Loss or mutation of Cbl‑c contributes to epithelial cancers, highlighting its importance in growth control and oncogenesis.

Cbl‑b is a single‑chain RING finger ubiquitin ligase that acts as a master regulator of immune activation. By ubiquitinating key signalling molecules in T‑cells, B‑cells and NK cells, Cbl‑b maintains immune tolerance and prevents hyperactivation. Loss of Cbl‑b leads to autoimmunity and enhanced anti‑tumour immunity, making it a critical player in immune homeostasis and a promising target in cancer immunotherapy.

The CBL family of ubiquitin ligases—c‑Cbl, Cbl‑b and Cbl‑c—are single‑chain RING finger E3 enzymes that regulate receptor tyrosine kinase signalling, immune activation and epithelial homeostasis. Through their TKB and RING domains, CBL proteins control ubiquitination, endocytosis and signal attenuation. Dysregulation of CBL ligases contributes to cancer, autoimmunity and inflammatory disorders, highlighting their importance in cellular regulation and disease.

c‑Cbl is a single‑chain RING finger ubiquitin ligase that regulates receptor tyrosine kinase signalling by binding phosphorylated RTKs and catalysing their ubiquitination. Through its TKB domain and RING domain, c‑Cbl controls EGFR turnover, immune signalling and cell growth. Mutations in c‑Cbl disrupt ubiquitination and contribute to myeloid malignancies, highlighting its importance in cellular homeostasis and disease.

Mdm2 is a RING‑type E3 ubiquitin ligase that controls p53 stability through ubiquitination, nuclear export and proteasomal degradation. By interacting with p53, Mdmx/Mdm4 and ARF, Mdm2 regulates DNA‑damage responses, cell‑cycle progression and oncogenesis, making it a central determinant of tumour development and genome stability.

Cdc25 phosphatases activate CDKs to drive both the G1–S and G2–M transitions. By removing inhibitory phosphates from CDK1 and CDK2, Cdc25 triggers DNA replication and mitotic entry. Checkpoint kinases such as Chk1 inhibit Cdc25 during DNA damage, while Cdc25 overexpression promotes genomic instability and contributes to tumour progression.