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CARD9

The protein encoded by this gene is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain (CARD). CARD is a protein interaction domain known to participate in activation or suppression of CARD containing members of the caspase family, and thus plays an important regulatory role in cell apoptosis. This protein was identified by its selective association with the CARD domain of BCL10, a postive regulator of apoptosis and NF-kappaB activation, and is thought to function as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-kappaB. Several alternatively spliced transcript variants have been observed, but their full-length nature is not clearly defined.
Protein class

Disease related genes, Human disease related genes

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Macrophages, Hofbauer cells, Kupffer cells, monocytes, Horizontal cells, Endometrial stromal cells, Langerhans cells)

Immune cell specificity

Immune cell enhanced (intermediate monocyte, non-classical monocyte)

Cell line specificity

Cell line enhanced (HEL, HMC-1, NB-4, THP-1)

Interaction

Monomer (PubMed:30206119). Homodimer; homodimerization is mediated by the CARD domain which forms an extensive interaction with the adjacent linker and coiled-coil regions; leads to an autoinhibited state (PubMed:30206119, PubMed:31296852). Homomultimer; polymerizes following activation, forming a nucleating helical template that seeds BCL10-filament formation via a CARD-CARD interaction (PubMed:31296852). Interacts (via CARD domain) with BCL10 (via CARD domain); interaction takes place following CARD9 activation and polymerization, leading to the formation of a filamentous CBM complex assembly (PubMed:11053425, PubMed:26488816, PubMed:31296852, PubMed:26521038). Component of a CBM complex (CARD9-BCL10, MALT1), composed of CARD9, BCL10 and MALT1 (PubMed:26521038). Interacts with RASGRF1 (PubMed:26521038). Interacts with NOD2 (via NACHT domain); interaction is direct (PubMed:24960071). Interacts with RIPK2 (By similarity). Interacts with VHL; without leading to protein degradation (By similarity).

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